Endoplasmic reticulum stress reduces the export from the ER and alters the architecture of post-ER compartments |
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| Authors: | Giuseppina Amodio Maurizio Renna Simona Paladino Consuelo Venturi Carlo Tacchetti Ornella Moltedo Silvia Franceschelli Massimo Mallardo Stefano Bonatti Paolo Remondelli |
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| Institution: | 1. Dipartimento di Scienze Farmaceutiche, Università degli Studi di Salerno, Via Ponte Don Melillo, Fisciano-Salerno I-84034, Italy;2. Dipartimento di Biologia e Patologia Cellulare e Molecolare, Università degli Studi di Napoli Federico II, 80131 Napoli, Italy;3. MicroSCoBiO Research Center and IFOM Center of Cell Oncology and Ultrastructure, Dipartimento di Medicina Sperimentale, Università di Genova, Italy;4. Dipartimento di Biochimica e Biotecnologie Mediche, Università degli Studi di Napoli “Federico II”, Naples I-80131, Italy;3. Institute of Biochemistry, Medical Faculty, Christian-Albrechts-University, 24098 Kiel, Germany;4. Institute of Biochemistry and Molecular Biology II, Medical Faculty, Heinrich-Heine-University, 40225 Düsseldorf, Germany;1. Hepatobiliary Department I, Hunan Provincial People''s Hospital (The first-affiliated hospital of Hunan normal university), The College of Clinical Medicine of Hunan Normal University, Changsha 410005, Hunan Province, PR China;2. Department of Nursing, Hunan Provincial People''s Hospital (The first-affiliated hospital of Hunan normal university), The College of Clinical Medicine of Hunan Normal University, Changsha 410005, Hunan Province, PR China;1. Université Saad Dahleb, Département des Sciences Agro-Vétérinaires et Biologiques, B.P. 270, route de Soumaa Blida, Algeria;2. Laboratoire d’Éco-Biologie Animale (L.E.B.A.); École Normale Supérieure de Kouba Bachir El Ibrahimi, B.P. 92, Algiers 6050, Algeria;3. Unitat de Bioquímica i Biologia Molecular, Facultat de Medicina, Institut d’Investigacións Biomèdiques (IDIBAPS), Universitat de Barcelona, CIBERNED, Spain |
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| Abstract: | In eukaryotic cells several physiologic and pathologic conditions generate the accumulation of unfolded proteins in the endoplasmic reticulum (ER), leading to ER stress. To restore normal function, some ER transmembrane proteins sense the ER stress and activate coordinated signalling pathways collectively called the Unfolded Protein Response (UPR). Little is known on how the UPR relates to post-ER compartments and to the export from the ER of newly synthesized proteins. Here, we report that the ER stress response induced by either thapsigargin or nitric oxide modifies the dynamics of the intracellular distribution of ERGIC-53 and GM130, two markers of the ER Golgi Intermediate Compartment and of the cis-Golgi, respectively. In addition, induction of ER stress alters the morphology of the ERGIC and the Golgi complex and interferes with the reformation of both compartments. Moreover, ER stress rapidly reduces the transport to the Golgi complex of the temperature sensitive mutant of the Vesicular Stomatitis Virus G Glycoprotein (VSV-G) fused with the Green Fluorescent Protein (ts045G), without apparently decreasing the amount of the protein competent for export. Interestingly, a parallel rapid reduction of the number of Sec31 labelled fluorescent puncta on the ER membranes does occur, thus suggesting that the ER stress alters the ER export and the dynamic of post-ER compartments by rapidly targeting the formation of COPII-coated transport intermediates. |
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